f 50The Lineweaver-Burk plot below depicts the effect of an inhibitor on the initial velocity (Vo) of anenzyme at different substrate concentrations [S] (with both values plotted as reciprocals and the lineextrapolated to negative values of [S]). Indicate whether the statements below are true or false:1akmulu/wrt of1VAXmax6 - 31/1²α=Slope1(S) (MM)[S]α = 2a=1No inhibitor=(1). DakmVmax 1akmBased on this diagram:15VmaxNo inhibitorSlope =[S] mmThe inhibitor increases the initial velocity of the enzymeThe inhibitor is not affecting the Vmax of the enzymeHOCJORDThe inhibitor is acting competitivelyAn increase in the inhibitor concentration results in a decrease in the apparentKm of the enzymeakmVmaxChoose...Choose...Choose... +Choose... #OReport question issueNot

Enzyme inhibition depends on the inhibitors and their action is seen by the Lineweaver Burk plot…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)
Given the following equations of the line, a) determine the KM of the substrate that binds the strongest with the enzyme. b) determine which of the following substrates binds the least with the enzyme
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches/Vm Vmax 2α' Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)
What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?
From a series of flasks with a constant concentration of enzyme the following initial velocities weretaken, they were obtained as a function of the concentration of the substrate.a) Calculate the KM and Vmax kinetic parameters of the three forms (Lineweaver-Burk, Eadie-Hofstee, Dixon).b) Analyze which are the atypical data that cause a low correlation, which can be eliminated and explain youranswer.
NOTE: the enzyme-inhibitor complex requires 450 joule/mol to dissociateJOULE/MOL
Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?
Given the assumption used to derive the Michaelis-Menten equation for enzyme kinetics that the back reaction from P + E back to ES does not occur, why is it important in measuring experimental data for Michaelis-Menten analysis to determine the initial rate of the reaction just after adding substrate to the sample being measured? O Because faster rates can be measured more accurately than slower rates later in the process. Because the Michaelis-Menten equation also contains the position of the equilibrium of the reaction. ● By using this approach, the amount of P at the start of the experiment is extremely low, causing the back reaction to be essentially absent. Because in this way the [ES] concentration has not yet reached steady state.

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depicts the effect of an inhibitor on the initial velocity (Vo) of an enzyme at different substrate concentrations [S] (with both values plotted as reciprocals and the line extrapolated to negative values of [S]). Indicate whether the statements below are true or false: